The post-translational modification landscape of commercial beers

Abstract Beer is one of the most popular beverages worldwide. As a product of variable agricultural ingredients and processes, beer has high molecular complexity. We used DIA/SWATH-MS to investigate the proteomic complexity and diversity of 23 commercial Australian beers. While the overall complexit...

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Autores principales: Edward D. Kerr, Christopher H. Caboche, Cassandra L. Pegg, Toan K. Phung, Claudia Gonzalez Viejo, Sigfredo Fuentes, Mark T. Howes, Kate Howell, Benjamin L. Schulz
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/c9d97b75257f40a181f8c3b9b9042c3e
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spelling oai:doaj.org-article:c9d97b75257f40a181f8c3b9b9042c3e2021-12-02T17:06:09ZThe post-translational modification landscape of commercial beers10.1038/s41598-021-95036-02045-2322https://doaj.org/article/c9d97b75257f40a181f8c3b9b9042c3e2021-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-95036-0https://doaj.org/toc/2045-2322Abstract Beer is one of the most popular beverages worldwide. As a product of variable agricultural ingredients and processes, beer has high molecular complexity. We used DIA/SWATH-MS to investigate the proteomic complexity and diversity of 23 commercial Australian beers. While the overall complexity of the beer proteome was modest, with contributions from barley and yeast proteins, we uncovered a very high diversity of post-translational modifications (PTMs), especially proteolysis, glycation, and glycosylation. Proteolysis was widespread throughout barley proteins, but showed clear site-specificity. Oligohexose modifications were common on lysines in barley proteins, consistent with glycation by maltooligosaccharides released from starch during malting or mashing. O-glycosylation consistent with oligomannose was abundant on secreted yeast glycoproteins. We developed and used data analysis pipelines to efficiently extract and quantify site-specific PTMs from SWATH-MS data, and showed incorporating these features into proteomic analyses extended analytical precision. We found that the key differentiator of the beer glyco/proteome was the brewery, with beer from independent breweries having a distinct profile to beer from multinational breweries. Within a given brewery, beer styles also had distinct glyco/proteomes. Targeting our analyses to beers from a single brewery, Newstead Brewing Co., allowed us to identify beer style-specific features of the glyco/proteome. Specifically, we found that proteins in darker beers tended to have low glycation and high proteolysis. Finally, we objectively quantified features of foam formation and stability, and showed that these quality properties correlated with the concentration of abundant surface-active proteins from barley and yeast.Edward D. KerrChristopher H. CabocheCassandra L. PeggToan K. PhungClaudia Gonzalez ViejoSigfredo FuentesMark T. HowesKate HowellBenjamin L. SchulzNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Edward D. Kerr
Christopher H. Caboche
Cassandra L. Pegg
Toan K. Phung
Claudia Gonzalez Viejo
Sigfredo Fuentes
Mark T. Howes
Kate Howell
Benjamin L. Schulz
The post-translational modification landscape of commercial beers
description Abstract Beer is one of the most popular beverages worldwide. As a product of variable agricultural ingredients and processes, beer has high molecular complexity. We used DIA/SWATH-MS to investigate the proteomic complexity and diversity of 23 commercial Australian beers. While the overall complexity of the beer proteome was modest, with contributions from barley and yeast proteins, we uncovered a very high diversity of post-translational modifications (PTMs), especially proteolysis, glycation, and glycosylation. Proteolysis was widespread throughout barley proteins, but showed clear site-specificity. Oligohexose modifications were common on lysines in barley proteins, consistent with glycation by maltooligosaccharides released from starch during malting or mashing. O-glycosylation consistent with oligomannose was abundant on secreted yeast glycoproteins. We developed and used data analysis pipelines to efficiently extract and quantify site-specific PTMs from SWATH-MS data, and showed incorporating these features into proteomic analyses extended analytical precision. We found that the key differentiator of the beer glyco/proteome was the brewery, with beer from independent breweries having a distinct profile to beer from multinational breweries. Within a given brewery, beer styles also had distinct glyco/proteomes. Targeting our analyses to beers from a single brewery, Newstead Brewing Co., allowed us to identify beer style-specific features of the glyco/proteome. Specifically, we found that proteins in darker beers tended to have low glycation and high proteolysis. Finally, we objectively quantified features of foam formation and stability, and showed that these quality properties correlated with the concentration of abundant surface-active proteins from barley and yeast.
format article
author Edward D. Kerr
Christopher H. Caboche
Cassandra L. Pegg
Toan K. Phung
Claudia Gonzalez Viejo
Sigfredo Fuentes
Mark T. Howes
Kate Howell
Benjamin L. Schulz
author_facet Edward D. Kerr
Christopher H. Caboche
Cassandra L. Pegg
Toan K. Phung
Claudia Gonzalez Viejo
Sigfredo Fuentes
Mark T. Howes
Kate Howell
Benjamin L. Schulz
author_sort Edward D. Kerr
title The post-translational modification landscape of commercial beers
title_short The post-translational modification landscape of commercial beers
title_full The post-translational modification landscape of commercial beers
title_fullStr The post-translational modification landscape of commercial beers
title_full_unstemmed The post-translational modification landscape of commercial beers
title_sort post-translational modification landscape of commercial beers
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/c9d97b75257f40a181f8c3b9b9042c3e
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